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HLDD_PHOLL
ID   HLDD_PHOLL              Reviewed;         312 AA.
AC   Q7MY46;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ADP-L-glycero-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE            EC=5.1.3.20 {ECO:0000255|HAMAP-Rule:MF_01601};
DE   AltName: Full=ADP-L-glycero-beta-D-manno-heptose-6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE            Short=ADP-glyceromanno-heptose 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE            Short=ADP-hep 6-epimerase {ECO:0000255|HAMAP-Rule:MF_01601};
DE            Short=AGME {ECO:0000255|HAMAP-Rule:MF_01601};
GN   Name=hldD {ECO:0000255|HAMAP-Rule:MF_01601}; Synonyms=rfaD;
GN   OrderedLocusNames=plu4847;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-
CC       manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an
CC       epimerization at carbon 6 of the heptose. {ECO:0000255|HAMAP-
CC       Rule:MF_01601}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-
CC         manno-heptose; Xref=Rhea:RHEA:17577, ChEBI:CHEBI:59967,
CC         ChEBI:CHEBI:61506; EC=5.1.3.20; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01601};
CC   -!- COFACTOR:
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01601};
CC       Note=Binds 1 NADP(+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01601};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC       heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC       glycero-beta-D-manno-heptose 7-phosphate: step 4/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01601}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_01601}.
CC   -!- DOMAIN: Contains a large N-terminal NADP-binding domain, and a smaller
CC       C-terminal substrate-binding domain. {ECO:0000255|HAMAP-Rule:MF_01601}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. HldD subfamily. {ECO:0000255|HAMAP-Rule:MF_01601}.
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DR   EMBL; BX571875; CAE17219.1; -; Genomic_DNA.
DR   RefSeq; WP_011148905.1; NC_005126.1.
DR   AlphaFoldDB; Q7MY46; -.
DR   SMR; Q7MY46; -.
DR   STRING; 243265.plu4847; -.
DR   PRIDE; Q7MY46; -.
DR   EnsemblBacteria; CAE17219; CAE17219; plu4847.
DR   GeneID; 24170658; -.
DR   KEGG; plu:plu4847; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_1_3_6; -.
DR   OMA; LRDFVYI; -.
DR   OrthoDB; 1180629at2; -.
DR   BioCyc; PLUM243265:PLU_RS24035-MON; -.
DR   UniPathway; UPA00356; UER00440.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0008712; F:ADP-glyceromanno-heptose 6-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05248; ADP_GME_SDR_e; 1.
DR   HAMAP; MF_01601; Heptose_epimerase; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR011912; Heptose_epim.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02197; heptose_epim; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; NADP; Reference proteome.
FT   CHAIN           1..312
FT                   /note="ADP-L-glycero-D-manno-heptose-6-epimerase"
FT                   /id="PRO_0000205804"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         10..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         31..32
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         38
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         75..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         92
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         144
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         178
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01601"
SQ   SEQUENCE   312 AA;  35396 MW;  EFF0B3405FB2CFB9 CRC64;
     MIIVTGGAGF IGSNIVKALN DEGYKDILVV DNLKDGTKFI NLADLDIADY MDKEEFIASI
     LAGDDFGDID AIFHEGACSS TTEWDGKYMM DNNYQYSKEL LHYCLERRTP FLYASSAATY
     GGRTDNFIEE RQYEKPLNVY GYSKFLFDQY VREILPQADS QICGFRYFNV YGPREGHKGS
     MASVAFHLNN QINQRQNPKL FAGSEGFQRD FIYVGDAAAV NLWFWKNGVS GIYNCGTGRA
     ESFQAVADAV VECHKDKSLT VEHIDFPEHL KGRYQRFTQA DLTKLRAAGY DKPFKTVAEG
     VTEYMHWLNQ DK
 
 
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